This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. ?-Synuclein remains a protein of interest due to its propensity to form fibrillar aggregates in Parkinson's Disease and its unknown functionality. ?-Synuclein localizes to synaptic vesicles, which are relatively small, with diameters of ~40 nm. Because of this small size the component lipids are under a curvature stress, which is relieved by fusion. We hypothesize that ?-Synuclein regulates synaptic vesicle fusion by relieving this curvature stress. Using all-atom molecular dynamics simulations we will examine the structure of ?-Synuclein [unreadable]membrane complexes and the affect of protein binding on membrane curvature.